title: Specificity patterns of different types of human fucosidase. Recognition of a certain region of the pyranose ring in sugars by the enzymes.
abstract: Data on the hydrolysis of fucosides, galactosides and arabinosides by different types of fucosidase are presented. The comparative study of the splitting of alpha-L-fucoside and beta-D-arabinoside with a similar structure at C1--C4 of the pyranose ring and the preparation of the enzyme by affinity chromatography showed that both substrates were hydrolysed by the same enzyme, alpha-L-fucoside(beta-D-arabinoside)hydrolase. The analogous investigation of the hydrolysis of beta-D-fucoside, beta-D-galactoside and alpha-L-arabinoside with a similar structure at C1--C4 of the pyranose ring demonstrated that these glycosides were split by the same enzyne, beta-D-fucoside(beta-D-galactoside, alpha-L-arabinoside)hydrolase, the activity of which is decreased dramatically in GM1-gangliosidosis. The data obtained support the assumption that the specific action of different types of fucosidase is due to recognition by these enzymes of C1--C4 of the pyranose ring in the corresponding substrates. The problems of differential diagnosis of some glycosidoses (focosidosis, GM1-gangliosidosis and Fabry disease) are discussed on the basis of the data obtained.
mesh_terms: D000328:Adult; D001665:Binding Sites; D002648:Child; D005260:Female; D005677:G(M1) Ganglioside; D005696:Galactosidases / Q000378:metabolism; D005697:Galactosides / Q000378:metabolism; D005733:Gangliosidoses / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000378:metabolism; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D007962:Leukocytes / Q000201:enzymology; D008297:Male; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D005644:alpha-L-Fucosidase / Q000378:metabolism*
chemical_list: D005697:Galactosides; D005677:G(M1) Ganglioside; D005696:Galactosidases; D006026:Glycoside Hydrolases; D005644:alpha-L-Fucosidase; C019713:alpha-N-arabinofuranosidase